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Volumn 60, Issue 9, 2012, Pages 2354-2361

Purification and characterization of a novel β-1,3-1,4-glucanase (lichenase) from thermophilic Rhizomucor miehei with high specific activity and its gene sequence

Author keywords

1,3 1,4 glucanase; Characterization; Gene cloning; Purification; Rhizomucor miehei

Indexed keywords

A-CARBON; AMINO ACID SEQUENCE; BIOCHEMICAL PROPERTIES; CRUDE ENZYMES; EXTRACELLULAR; GEL FILTRATION; GENE CLONING; GENE SEQUENCES; HIGH-LEVEL PRODUCTION; PAECILOMYCES; PURIFIED ENZYME; RHIZOMUCOR MIEHEI; SPECIFIC ACTIVITY;

EID: 84859774681     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf2049799     Document Type: Article
Times cited : (55)

References (32)
  • 1
    • 77951092898 scopus 로고    scopus 로고
    • Biochemical characterization of a maize stover β-exoglucanase and its use in lignocelluloses conversion
    • Han, Y. J.; Chen, H. Z. Biochemical characterization of a maize stover β-exoglucanase and its use in lignocelluloses conversion. Bioresour. Technol. 2010, 101, 6111-6117.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6111-6117
    • Han, Y.J.1    Chen, H.Z.2
  • 3
    • 0034863407 scopus 로고    scopus 로고
    • Structure-function relationships of β-D-glucan endo- and exohydrolases from higher plants
    • DOI 10.1023/A:1010619128894
    • Hrmova, M.; Fincher, G. B. Structure-function relationships of β- D-glucan endo- and exohydrolases from higher plants. Plant Mol. Biol. 2001, 47, 73-91. (Pubitemid 32804498)
    • (2001) Plant Molecular Biology , vol.47 , Issue.1-2 , pp. 73-91
    • Hrmova, M.1    Fincher, G.B.2
  • 4
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial β-1,3-1,4-glucanase: Structure, function and protein engineering
    • Planas, A. Bacterial β-1,3-1,4-glucanase: structure, function and protein engineering. Biochim. Biophys. Acta 2000, 1543, 361-382.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 5
    • 1642446551 scopus 로고    scopus 로고
    • Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF A5 using response surface methodology
    • Tang, X. J.; Guo, Q. H.; Chen, Q. H.; Zhang, X. Y.; Ali, M. A. M. Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF A5 using response surface methodology. Bioresour. Technol. 2004, 93, 175-183.
    • (2004) Bioresour. Technol. , vol.93 , pp. 175-183
    • Tang, X.J.1    Guo, Q.H.2    Chen, Q.H.3    Zhang, X.Y.4    Ali, M.A.M.5
  • 6
    • 33749009721 scopus 로고    scopus 로고
    • Cloning of β-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3)
    • DOI 10.1007/s00253-006-0329-2
    • Teng, D.; Wang, J. H.; Fan, Y.; Yang, Y. L.; Tian, Z. G.; Luo, J.; Yang, G. P.; Zhang, F. Cloning of β-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039(CGMCC 0635) and its expression in Eschrichia coli BL21 (DE3). Appl. Microbiol. Biotechnol. 2006, 72 (4), 705-712. (Pubitemid 44454930)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.4 , pp. 705-712
    • Teng, D.1    Wang, J.-H.2    Fan, Y.3    Yang, Y.-L.4    Tian, Z.-G.5    Luo, J.6    Yang, G.-P.7    Zhang, F.8
  • 7
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • DOI 10.1016/S0141-0229(01)00354-4, PII S0141022901003544
    • Murray, P. G.; Grassick, A.; Laffey, C. D.; Cuffe, M. M.; Higgins, T.; Savage, A. V.; Planas, A.; Tuohy, M. G. Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microb. Technol. 2001, 29, 90-98. (Pubitemid 32566389)
    • (2001) Enzyme and Microbial Technology , vol.29 , Issue.1 , pp. 90-98
    • Murray, P.G.1    Grassick, A.2    Laffey, C.D.3    Cuffe, M.M.4    Higgins, T.5    Savage, A.V.6    Planas, A.7    Tuohy, M.G.8
  • 8
    • 33845688815 scopus 로고    scopus 로고
    • Characterization of a β-glucanase produced by Rhizopus microspores var. microspores, and its potential for application in the brewing industry
    • Celestino, K. R. S.; Cunha, R. B.; Felix, C. R. Characterization of a β-glucanase produced by Rhizopus microspores var. microspores, and its potential for application in the brewing industry. BMC Biochem. 2006, 7, 23.
    • (2006) BMC Biochem. , vol.7 , pp. 23
    • Celestino, K.R.S.1    Cunha, R.B.2    Felix, C.R.3
  • 9
    • 33748145628 scopus 로고    scopus 로고
    • Purification and characterization of two endoglucanases from Melanocarpus sp. MTCC 3922
    • DOI 10.1016/j.biortech.2005.11.019, PII S0960852405005444
    • Kaur, J.; Chadha, B. S.; Kumar, B. A.; Saini, H. S. Purification and characterization of two endoglucanases from Melanocarpus sp. MTCC 3922. Bioresour. Technol. 2007, 98, 74-81. (Pubitemid 44314095)
    • (2007) Bioresource Technology , vol.98 , Issue.1 , pp. 74-81
    • Kaur, J.1    Chadha, B.S.2    Kumar, B.A.3    Saini, H.S.4
  • 10
    • 70849094923 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable β-1,3-1,4- glucanase from Laetiporus sulphureus var miniatus
    • Hong, M. R.; Kim, Y. S.; Joo, A. R.; Lee, J. K.; Kim, Y. S.; Oh, D. K. Purification and characterization of a thermostable β-1,3-1,4-glucanase from Laetiporus sulphureus var miniatus. J. Microbiol. Biotechnol. 2009, 19, 818-822.
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 818-822
    • Hong, M.R.1    Kim, Y.S.2    Joo, A.R.3    Lee, J.K.4    Kim, Y.S.5    Oh, D.K.6
  • 12
    • 47849101161 scopus 로고    scopus 로고
    • Biochemical characterization of a novel thermostable β-1,3-1,4- glucanase (Lichenase) from Paecilomyces thermophila
    • DOI 10.1021/jf800303b
    • Yang, S. Q.; Yan, Q. J.; Jiang, Z. Q.; Fan, G. S.; Wang, L. Biochemical characterization of a novel thermostable β-1,3-1,4- glucanase (lichenase) from Paecilomyces thermophila. J. Agric. Food Chem. 2008, 56 (13), 5345-5351. (Pubitemid 352039145)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.13 , pp. 5345-5351
    • Yang, S.1    Qiaojuan, Y.2    Jiang, Z.3    Fan, G.4    Wang, L.5
  • 15
    • 34548295727 scopus 로고    scopus 로고
    • Production, purification and application-relevant characterisation of an endo-1,3(4)-β-glucanase from Rhizomucor miehei
    • DOI 10.1007/s00253-007-1058-x
    • Boyce, A.; Walsh, G. Production, purification and applicationrelevant characterization of an endo-β-1,3(4)-glucanase from Rhizomucor miehei. Appl. Microbiol. Biotechnol. 2007, 76, 835-841. (Pubitemid 47340938)
    • (2007) Applied Microbiology and Biotechnology , vol.76 , Issue.4 , pp. 835-841
    • Boyce, A.1    Walsh, G.2
  • 17
    • 79952562966 scopus 로고    scopus 로고
    • Highly thermostable xylanase purified from Rhizomucor miehei NRL 3169
    • Fawzi, E. M. Highly thermostable xylanase purified from Rhizomucor miehei NRL 3169. Acta Biol. Hung. 2011, 62, 85-94.
    • (2011) Acta Biol. Hung. , vol.62 , pp. 85-94
    • Fawzi, E.M.1
  • 18
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey, M. J.; Biely, P.; Poutanen, K. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 1992, 23, 257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 19
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31, 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0014548372 scopus 로고
    • Glycoprotein staining following electrophoresis on acrylamide gels
    • Zacharius, R. M.; Zell, T. E.; Morrison, J. H.; Woodlock, J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal. Biochem. 1969, 30, 148-152.
    • (1969) Anal. Biochem. , vol.30 , pp. 148-152
    • Zacharius, R.M.1    Zell, T.E.2    Morrison, J.H.3    Woodlock, J.J.4
  • 23
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rebe, P. A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebe, P.A.4    Smith, F.5
  • 25
    • 0032052770 scopus 로고    scopus 로고
    • Consensus-degenerate hybrid oligonucleotide primers for amplification of distantly related sequences
    • DOI 10.1093/nar/26.7.1628
    • Rose, T. M.; Schultz, E. R.; Henikoff, J. G.; Pietrokovski, S.; McCallum, C. M.; Henikoff, S. Consensus degenerate hybrid oligonucleotide primers for amplification of distantly related sequences. Nucleic Acids Res. 1998, 26, 1628-1635. (Pubitemid 28291796)
    • (1998) Nucleic Acids Research , vol.26 , Issue.7 , pp. 1628-1635
    • Rose, T.M.1    Schultz, E.R.2    Henikoff, J.G.3    Pietrokovski, S.4    McCallum, C.M.5    Henikoff, S.6
  • 26
    • 0030883632 scopus 로고    scopus 로고
    • Sequencing of a 1,3-1,4-β-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: Properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin
    • Chen, H.; Li, X. L.; Ljungdahl, L. G. Sequencing of a 1,3-1,4-β- D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin. J. Bacteriol. 1997, 179, 6028-6034. (Pubitemid 27419025)
    • (1997) Journal of Bacteriology , vol.179 , Issue.19 , pp. 6028-6034
    • Chen, H.1    Li, X.-L.2    Ljungdahl, L.G.3
  • 27
    • 0042412981 scopus 로고    scopus 로고
    • Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum
    • Görlach, J. M.; Knaap, E. V. D.; Walton, J. D. Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochlibolus carbonum. Appl. Environ. Microbiol. 1998, 64, 385-391. (Pubitemid 28079794)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.2 , pp. 385-391
    • Gorlach, J.M.1    Van Der Knaap, E.2    Walton, J.D.3
  • 28
    • 29944444016 scopus 로고    scopus 로고
    • A lichenase-like family 12 endo-(1?4)-β-glucanase from Aspergillus japonicas: Study of the substrate specificity and mode of action on β- glucans in comparison with other glycoside hydrolases
    • DOI 10.1016/j.carres.2005.11.011, PII S0008621505005112
    • Grishutin, S. G.; Gusakov, A. V.; Dzedzyulya, E. I.; Sinitsyn, A. P. A lichenase-like family 12 endo-(1?4)-β-glucanase from Aspergillus japonicas: study of the substrate specificity and mode of action on β- glucans in comparison with other glycoside hydrolases. Carbohydr. Res. 2006, 341, 218-229. (Pubitemid 43042605)
    • (2006) Carbohydrate Research , vol.341 , Issue.2 , pp. 218-229
    • Grishutin, S.G.1    Gusakov, A.V.2    Dzedzyulya, E.I.3    Sinitsyn, A.P.4
  • 29
    • 0037102477 scopus 로고    scopus 로고
    • Biochmical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus
    • Parry, N. J.; Beever, D. E.; Owen, E.; Nerinckx, W.; Claeyssens, M.; Beeumen, J. V.; Bhat, M. K. Biochmical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Arch. Biochem. Biophys. 2002, 404, 242-253.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 242-253
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Nerinckx, W.4    Claeyssens, M.5    Beeumen, J.V.6    Bhat, M.K.7
  • 30
    • 21744452510 scopus 로고    scopus 로고
    • A truncated Fibrobacter succinogenes 1,3-1,4-β-glucanase with improved enzymatic activity and thermotolerance
    • Wen, T. N.; Chen, J. L.; Lee, S. H.; Yang, N. S.; Shyur, L. F. A truncated Fibrobacter succinogenes 1,3-1,4-β-glucanase with improved enzymatic activity and thermotolerance. Biochemistry 2005, 44, 9197-9205.
    • (2005) Biochemistry , vol.44 , pp. 9197-9205
    • Wen, T.N.1    Chen, J.L.2    Lee, S.H.3    Yang, N.S.4    Shyur, L.F.5
  • 31
    • 52049115933 scopus 로고    scopus 로고
    • Grass degrading β-1,3-1,4-D-glucanases from Bacillus subtilis GN156: Purification and characterization of glucanase J1 and pJ2 possessing extremely acidic pI
    • Apiraksakorn, J.; Nitisinprasert, T.; Levin, R. E. Grass degrading β-1,3-1,4-D-glucanases from Bacillus subtilis GN156: purification and characterization of glucanase J1 and pJ2 possessing extremely acidic pI. Appl. Biochem. Biotechnol. 2008, 149, 53-66.
    • (2008) Appl. Biochem. Biotechnol. , vol.149 , pp. 53-66
    • Apiraksakorn, J.1    Nitisinprasert, T.2    Levin, R.E.3
  • 32
    • 33947275929 scopus 로고    scopus 로고
    • Codon optimization of Bacillus licheniformis β-1,3-1,4-glucanase gene and its expression in Pichia pastoris
    • Teng, D.; Fan, Y.; Yang, Y. L.; Tian, Z. G.; Luo, J.; Wang, J. H. Codon optimization of Bacillus licheniformis β-1,3-1,4-glucanase gene and its expression in Pichia pastoris. Appl. Microbiol. Biotechnol. 2007, 74, 705-712.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 705-712
    • Teng, D.1    Fan, Y.2    Yang, Y.L.3    Tian, Z.G.4    Luo, J.5    Wang, J.H.6


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